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Article

Cytoplasmic tail phosphorylation of the alpha-factor receptor is required for its ubiquitination and internalization.

The Journal of cell biology - 20 Apr 1998

Hicke L, Zanolari B, Riezman H

Abstract excerpt

G protein-coupled (GPC) receptors are phosphorylated in response to ligand binding, a modification that promotes receptor desensitization or downregulation. The alpha-factor pheromone receptor (Ste2p) of Saccharomyces cerevisiae is a GPC receptor that is hyperphosphorylated and ubiquitinated upon binding alpha-factor. Ubiquitination triggers Ste2p internalization into the endocytic pathway. Here we demonstrate...

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Identifiers

PMID: 9548714
DOI: 10.1083/jcb.141.2.349
PMCID: PMC2148449

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Cytoplasmic tail phosphorylation of the alpha-factor receptor is required for its ubiquitination and internalization.PMID 9548714Read ↗

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Ubiquitination of the yeast a-factor receptor.Semantic proximity Read ↗

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Identification of a novel sequence mediating regulated endocytosis of the G protein-coupled alpha-pheromone receptor in yeast.Semantic proximity Read ↗

Direct evidence for ligand-induced internalization of the yeast alpha-factor pheromone receptor.Semantic proximity Read ↗

The C terminus of the Saccharomyces cerevisiae alpha-factor receptor contributes to the formation of preactivation complexes with its cognate G protein.Semantic proximity Read ↗

Homo-oligomeric complexes of the yeast alpha-factor pheromone receptor are functional units of endocytosis.Semantic proximity Read ↗

Dynamic ubiquitination of the mitogen-activated protein kinase kinase (MAPKK) Ste7 determines mitogen-activated protein kinase (MAPK) specificity.Semantic proximity Read ↗

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